1pwa
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Revision as of 16:41, 12 November 2007
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Crystal structure of Fibroblast Growth Factor 19
Overview
The 22 members of the FGF family have been implicated in cell, proliferation, differentiation, survival, and migration. They are required, for both development and maintenance of vertebrates, demonstrating an, exquisite pattern of affinities for both protein and proteoglycan, receptors. FGF19, one of the most divergent human FGFs, is unique in, binding solely to one receptor, FGFR4. We have used molecular replacement, to solve the crystal structure of FGF19 at 1.3 A resolution using five, superimposed FGF structures as the search model. The structure shows that, two novel disulfide bonds found in FGF19, one of which appears to be, conserved among several of the other FGFs, stabilize extended loops. The, key heparin-binding loops of FGF19 have radically different conformations, and charge patterns, compared to other FGFs, correlating with the, unusually low affinity of FGF19 for heparin. A model for the complex of, FGF19 with FGFR4 demonstrates that unique sequences in both FGF19 and, FGFR4 are key to the formation of the complex. The structure therefore, offers a clear explanation for the unusual affinity of FGF19 for FGFR4, alone.
About this Structure
1PWA is a Single protein structure of sequence from Homo sapiens with SO4, TRS and GOL as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of fibroblast growth factor (FGF) 19 reveals novel features of the FGF family and offers a structural basis for its unusual receptor affinity., Harmer NJ, Pellegrini L, Chirgadze D, Fernandez-Recio J, Blundell TL, Biochemistry. 2004 Jan 27;43(3):629-40. PMID:14730967
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